Competitive binding of phenylbutazone and colchicine to serum albumin in multidrug therapy: A spectroscopic study

Sułkowska, Anna; Maciążek-Jurczyk, Małgorzata; Bojko, Barbara; Równicka, J.; Zubik-Skupień, I.; Temba, E.; Pentak, Danuta; Sułkowski, Wieslaw W.

doi:10.1016/j.molstruc.2007.09.001

Cited by 119 publications

(61 citation statements)

References 29 publications

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“…Quinolone derivatives, antibacterial drugs, are widely used in the chemotherapy of various infectious diseases, especially against Gram-negative bacteria, with broader spectrum and greater actively compared to nalidixic and oxolinic acid [12,13]. The medicinal functions have extensively been studied [14], and proved to prevent bacterial DNA biosynthesis by inhibiting the bacterial enzyme DNA gyrase [15,16]. In the interest of enriching the information database of such research, we chose lomefloxacin (LMF) as a donor, which is a typical representation of quinolones.…”

Section: Introductionmentioning

confidence: 99%

Characterization of the interaction between human lactoferrin and lomefloxacin at physiological condition: Multi-spectroscopic and modeling description

Chamani

Tafrishi

Momen-Heravi

2010

Journal of Luminescence

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Section: Introductionmentioning

confidence: 99%

Characterization of the interaction between human lactoferrin and lomefloxacin at physiological condition: Multi-spectroscopic and modeling description

Chamani

Tafrishi

Momen-Heravi

2010

Journal of Luminescence

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“…Thus, it is important to understand not only how much drug is bound to protein, but also the site-specificity and the nature of forces involved in the binding of these agents with serum albumin, the major drug binding protein in blood plasma. Fluorescence spectroscopy, due to its exceptional sensitivity, selectivity and sound theoretical foundation [6], is a convenient method for studying drug-protein interaction [7][8]. In the present work, the mechanism of interaction and detailed physico-chemical characterization of the binding of glimepiride and glipizide with human serum albumin Mechanism of interaction of hypoglycemic agents glimepiride and glipizide with human serum albumin has been studied using fluorescence spectroscopy.…”

Section: Introductionmentioning

confidence: 99%

Mechanism of interaction of hypoglycemic agents glimepiride and glipizide with human serum albumin

Seedher

Kanojia

2009

Open Chemistry

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Abstract:The mechanism of interaction of hypoglycemic drugs, glimepiride and glipizide with human serum albumin (HSA) has been studied using fluorescence spectroscopy. The results are discussed in terms of the binding parameters, thermodynamics of the binding process, nature of forces involved in the interaction, identification of drug binding site on serum albumin and the fluorescence quenching mechanism involved. The association constants were of the order of 10 5 and glipizide was found to have much higher affinity for HSA than glimepiride at all temperatures. Thermodynamic parameters for the binding suggested that hydrophobic interactions are primarily involved in the binding of these drugs to HSA. However, glimepiride and glipizide appear to cause temperature-dependent conformational changes in the albumin molecule and, therefore, the nature of interaction varied with temperature. Glimepiride and glipizide bind to both site I and site II on HSA, but the primary interaction occurs at site II. The binding region in site II is different for the two drugs. Stern-Volmer analysis of quenching data indicated that tryptophan residues of HSA are not fully accessible to the drugs and a predominantly dynamic quenching mechanism is involved in the binding. Results can provide useful insight into prediction of competitive displacement of these drugs by other co-administered drugs and excipients, resulting in serious fluctuations of the blood glucose levels in diabetic patients.

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“…12,13,14,15 This however is dependent upon the dose of colchicine and duration of treatment; the effect is at both molecular and genetic level. 25 The competitive binding of colchicine to serum albumin was well established 26 and thus supports the selection of appropriate method in study to check the existing variability in targeted pharmaco logical activity. Quantification data reveals significant variation in the colchicine content of collected samples, among which NBG-128 was statistically selected as the elite chemotype with high colchicine content.…”

Section: Discussionmentioning

confidence: 83%

Evaluation of Anti Arthritic Potential of Gloriosa superba (L.) Elite Germplasm Collected from Eastern Himalayas, India

Misra¹,

Srivastava²,

Khalid³

et al. 2017

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Competitive binding of phenylbutazone and colchicine to serum albumin in multidrug therapy: A spectroscopic study

Cited by 119 publications

References 29 publications

Characterization of the interaction between human lactoferrin and lomefloxacin at physiological condition: Multi-spectroscopic and modeling description

Characterization of the interaction between human lactoferrin and lomefloxacin at physiological condition: Multi-spectroscopic and modeling description

Mechanism of interaction of hypoglycemic agents glimepiride and glipizide with human serum albumin

Evaluation of Anti Arthritic Potential of Gloriosa superba (L.) Elite Germplasm Collected from Eastern Himalayas, India

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